Chlorine in PDB 3gky: The Structural Basis of An Er Stress-Associated Bottleneck in A Protein Folding Landscape

The structure of The Structural Basis of An Er Stress-Associated Bottleneck in A Protein Folding Landscape, PDB code: 3gky was solved by M.Liu, Z.L.Wan, Y.C.Chu, H.Alddin, B.Klaproth, M.A.Weiss, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	22.58 / 1.80
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	78.225, 78.225, 36.712, 90.00, 90.00, 120.00
R / Rfree (%)	20.9 / 25.3

The structure of The Structural Basis of An Er Stress-Associated Bottleneck in A Protein Folding Landscape also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Chlorine atom in the The Structural Basis of An Er Stress-Associated Bottleneck in A Protein Folding Landscape (pdb code 3gky). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the The Structural Basis of An Er Stress-Associated Bottleneck in A Protein Folding Landscape, PDB code: 3gky:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the The Structural Basis of An Er Stress-Associated Bottleneck in A Protein Folding Landscape


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of The Structural Basis of An Er Stress-Associated Bottleneck in A Protein Folding Landscape within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl32 b:38.9 occ:0.33 ZN B:ZN31 2.3 28.9 0.3 O B:HOH89 3.0 51.1 1.0 NE2 B:HIS10 3.8 20.4 1.0 CD2 B:HIS10 4.2 22.8 1.0 CE1 B:HIS10 5.0 21.9 1.0

Chlorine binding site 2 out of 2 in the The Structural Basis of An Er Stress-Associated Bottleneck in A Protein Folding Landscape


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of The Structural Basis of An Er Stress-Associated Bottleneck in A Protein Folding Landscape within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl32 b:20.7 occ:0.33 ZN D:ZN31 2.2 19.7 0.3 NE2 D:HIS10 3.4 21.7 1.0 CB D:LEU6 3.8 23.3 1.0 CD1 D:LEU6 3.9 25.8 1.0 CD2 D:HIS10 4.1 20.9 1.0 CE1 D:HIS10 4.3 26.1 1.0 CG D:LEU6 4.4 22.3 1.0 CA D:LEU6 4.9 24.0 1.0 C D:LEU6 4.9 24.4 1.0 O D:LEU6 4.9 23.6 1.0

M.Liu, Z.L.Wan, Y.C.Chu, H.Aladdin, B.Klaproth, M.Choquette, Q.X.Hua, R.B.Mackin, J.S.Rao, P.De Meyts, P.G.Katsoyannis, P.Arvan, M.A.Weiss. Crystal Structure of A "Nonfoldable" Insulin: Impaired Folding Efficiency Despite Native Activity. J.Biol.Chem. V. 284 35259 2009.
ISSN: ISSN 0021-9258
PubMed: 19850922
DOI: 10.1074/JBC.M109.046888